ArticleMicrobial cell factories2017
A novel Ffu fusion system for secretory expression of heterologous proteins in Escherichia coli.
Article in Microbial cell factories, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed, 19 citations in OpenAlex.
- Cosolvent-induced spontaneous refolding of lipase.Applied microbiology and biotechnology · 2026Article
- In situ formed depot of elastin-like polypeptide-hirudin fusion protein for long-acting antithrombotic therapy.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Recent Advances in the Synthetic Biology of Natural Drugs.Frontiers in bioengineering and biotechnology · 2021Review
- Polyionic Tags as Enhancers of Protein Solubility in Recombinant Protein Expression.Microorganisms · 2018Review
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6 authors at 2 institutions in 1 country.
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Abstract
backgroundThe high level of excretion and rapid folding ability of β-fructofuranosidase (β-FFase) in Escherichia coli has suggested that β-FFase from Arthrobacter arilaitensis NJEM01 can be developed as a fusion partner.
methodsBased on the modified Wilkinson and Harrison algorithm and the preliminary verification of the solubility-enhancing ability of β-FFase truncations, three β-FFase truncations (i.e., Ffu209, Ffu217, and Ffu312) with a native signal peptide were selected as novel Ffu fusion tags. Four difficult-to-express protein models; i.e., CARDS TX, VEGFR-2, RVs and Omp85 were used in the assessment of Ffu fusion tags.
resultsThe expression levels and solubility of each protein were markedly enhanced by the Ffu fusion system. Each protein had a favorable Ffu tag. The Ffu fusion tags performed preferably when compared with the well-known fusion tags MBP and NusA. Strikingly, it was confirmed that Ffu fusion proteins were secreted into the periplasm by the periplasmic analysis and N-amino acid sequence analysis. Further, efficient excretion of HV3 with defined anti-thrombin activity was obtained when it was fused with the Ffu312 tag. Moreover, HV3 remained soluble and demonstrated notable anti-thrombin activity after the removal of the Ffu312 tag by enterokinase.
conclusionsObservations from this work not only complements fusion technologies, but also develops a novel and effective secretory system to solve key issues that include inclusion bodies and degradation when expressing heterologous proteins in E. coli, especially for proteins that require disulfide bond formation, eukaryotic-secreted proteins, and membrane-associated proteins.
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